1cz7
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THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS
OverviewOverview
BACKGROUND: The kinesin superfamily of microtubule-associated motor, proteins are important for intracellular transport and for cell division, in eukaryotes. Conventional kinesins have the motor domain at the N, terminus of the heavy chain and move towards the plus end of microtubules., The ncd protein is necessary for chromosome segregation in meiosis. It, belongs to a subfamily of kinesins that have the motor domain at the C, terminus and move towards the minus end of microtubules. RESULTS: The, crystal structure of dimeric ncd has been obtained at 2.9 A resolution, from crystals with the C222(1) space group, with two independent dimers, per asymmetric unit. The motor domains in these dimers are not related by, crystallographic symmetry and the two ncd dimers have significantly, different conformations. An alpha-helical coiled coil connects, and, interacts with, the motor domains. CONCLUSIONS: The ncd protein has a very, compact structure, largely due to extended interactions of the coiled coil, with the head domains. Despite this, we find that the overall conformation, of the ncd dimer can be rotated by as much as 10 degrees away from that of, the twofold-symmetric archetypal ncd. The crystal structures of, conventional kinesin and of ncd suggest a structural rationale for the, reversal of the direction of movement in chimeric kinesins.
About this StructureAbout this Structure
1CZ7 is a Single protein structure of sequence from Drosophila melanogaster with MG and ADP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations., Kozielski F, De Bonis S, Burmeister WP, Cohen-Addad C, Wade RH, Structure. 1999 Nov 15;7(11):1407-16. PMID:10574799
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